The RNA methyltransferase METTL8 installs m3C32 in mitochondrial tRNAsThr/Ser(UCN) to optimise tRNA structure and mitochondrial translation

Autor: Nicole Kleiber, Nicolas Lemus-Diaz, Carina Stiller, Marleen Heinrichs, Mandy Mong-Quyen Mai, Philipp Hackert, Ricarda Richter-Dennerlein, Claudia Höbartner, Katherine E. Bohnsack, Markus T. Bohnsack

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-19 (2022)

RNA modifications are key regulators of RNA functions. Here, the authors identify METTL8 as the enzyme installing m3C32 in mitochondrial tRNAThr/Ser(UCN). Lack of these modifications affects tRNA structure and impairs mitochondrial translation.

Externí odkaz: https://doaj.org/article/b66a7c73278d4acdb1a5947679641b80

Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast

Autor: Ying Zhang, Evelina De Laurentiis, Katherine E. Bohnsack, Mascha Wahlig, Namit Ranjan, Simon Gruseck, Philipp Hackert, Tina Wölfle, Marina V. Rodnina, Blanche Schwappach, Sabine Rospert

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021)

The guided entry of tail-anchored proteins (GET) pathway assists in the delivery of such proteins to the ER. Here, the authors reveal that the pathway components Get4/5 probe a region near the ribosomal exit tunnel. Upon emergence of a client protein

Externí odkaz: https://doaj.org/article/96ddf33632654134a1b5c75874d99b55

RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes

Autor: Lukas Brüning, Philipp Hackert, Roman Martin, Jimena Davila Gallesio, Gerald Ryan R. Aquino, Henning Urlaub, Katherine E. Sloan, Markus T. Bohnsack

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)

Pre-ribosomes undergo numerous structural rearrangements during their assembly. Here the authors identify the binding sites of three essential RNA helicases on pre-ribosomal particles, enabling them to provide insights into the structural and composi

Externí odkaz: https://doaj.org/article/60281cffa46941bcbffe87e438136b67

The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

Autor: Anthony K. Henras, Nicolai Krogh, Mariam Jaafar, Gerald Ryan R. Aquino, Henrik Nielsen, Katherine E. Bohnsack, Philipp Hackert, Kuan-Ting Pan, Markus T. Bohnsack, Henning Urlaub

Publikováno v: Nature Communications
Aquino, G R R, Hackert, P, Krogh, N, Pan, K T, Jaafar, M, Henras, A K, Nielsen, H, Urlaub, H, Bohnsack, K E & Bohnsack, M T 2021, ' The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly ', Nature Communications, vol. 12, 6152 . https://doi.org/10.1038/s41467-021-26208-9
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)

Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numero

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4ea361f622bea0e17b92b23c9ff043a
https://doi.org/10.1038/s41467-021-26208-9

The RNA methyltransferase METTL8 installs m

Autor: Nicole, Kleiber, Nicolas, Lemus-Diaz, Carina, Stiller, Marleen, Heinrichs, Mandy Mong-Quyen, Mai, Philipp, Hackert, Ricarda, Richter-Dennerlein, Claudia, Höbartner, Katherine E, Bohnsack, Markus T, Bohnsack

Publikováno v: Nature Communications

Modified nucleotides in tRNAs are important determinants of folding, structure and function. Here we identify METTL8 as a mitochondrial matrix protein and active RNA methyltransferase responsible for installing m3C32 in the human mitochondrial (mt-)t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ad1fbf0e95915065a0be5efabf499a99
https://pubmed.ncbi.nlm.nih.gov/35017528